{"gene":"PF3D7_0909200","run_date":"2026-09-08T12:51:27","timeline":{"discoveries":[{"year":2003,"finding":"POFUT2 (protein O-fucosyltransferase family 2) was identified as a member of a new superfamily of fucosyltransferases sharing three conserved peptide motifs with alpha2-fucosyltransferases, alpha6-fucosyltransferases, and POFUT1, suggesting origin from a common ancestor by gene duplication and divergent evolution.","method":"Phylogenetic analysis and identification of conserved peptide motifs across fucosyltransferase families","journal":"Glycobiology","confidence":"Low","confidence_rationale":"Tier 4 / Weak — computational/comparative sequence analysis only, no in vitro or in vivo functional experiment performed on the Plasmodium POFUT2 protein itself","pmids":["12966037"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"finding":"POFUT2 (PF3D7_0909200) is the Plasmodium O-fucosyltransferase responsible for O-glycosylating the thrombospondin repeat (TSR)-containing sporozoite surface proteins CSP and TRAP. Genetic disruption of POFUT2 in P. falciparum produced ookinetes attenuated for mosquito midgut colonization, and POFUT2-deficient sporozoites were impaired for gliding motility, cell traversal, hepatocyte invasion, and production of exoerythrocytic forms in humanized chimeric liver mice. These defects were attributed to destabilization and incorrect trafficking of TSR-bearing proteins, placing POFUT2 in a non-canonical glycosylation-dependent ER protein quality control mechanism.","method":"Genetic disruption (knockout) of POFUT2 in P. falciparum; phenotyping across the full parasite life cycle; assessment of CSP/TRAP stability and trafficking","journal":"Nature communications","confidence":"High","confidence_rationale":"Tier 2 / Strong — clean genetic knockout with multiple orthogonal phenotypic readouts (motility, invasion, trafficking, in vivo infection) across distinct life-cycle stages; mechanistic link to TSR protein quality control established","pmids":["28916755"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2019,"finding":"POFUT2 null-mutant P. berghei parasites showed no deleterious motility phenotypes and successfully established blood-stage infection in mice, indicating that POFUT2-mediated O-fucosylation of TSR domains is not essential for P. berghei development in contrast to findings in P. falciparum.","method":"Genetic disruption (null mutant generation) of POFUT2 in P. berghei; full life-cycle phenotyping including sporozoite motility assays and mouse infection","journal":"Frontiers in cellular and infection microbiology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — clean genetic knockout with multiple phenotypic assays in a rodent malaria model, but contradicts P. falciparum findings and one subsequent P. berghei study; single-lab result","pmids":["31334132"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2024,"finding":"Disruption of POFUT2 in P. berghei resulted in sporozoites with reduced TRAP protein levels, impaired gliding motility, and diminished hepatocyte infectivity in mice, while blood and mosquito stages developed normally. All-atom molecular dynamics simulation suggested O-fucosylation stabilizes the TSR domain structure rather than affecting its heparin-binding capacity.","method":"POFUT2 gene disruption (KO) in P. berghei; quantification of TRAP protein levels; gliding motility and hepatocyte invasion assays; all-atom MD simulation of TSR domain","journal":"ACS infectious diseases","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — genetic knockout with mechanistic follow-up (TRAP quantification, motility assay, invasion assay) in a rodent malaria model; MD simulation is computational and hypothesis-generating; single lab, partially contradicts PMID:31334132","pmids":["38421807"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]}],"current_model":"POFUT2 (PF3D7_0909200) is a GDP-fucose protein O-fucosyltransferase that O-glycosylates thrombospondin type I repeat (TSR)-containing proteins, including the sporozoite surface proteins CSP and TRAP; in P. falciparum, this modification is required for proper TSR protein folding, stability, and ER-dependent trafficking, and its loss severely attenuates mosquito midgut colonization, sporozoite gliding motility, hepatocyte invasion, and liver-stage development, whereas in P. berghei the phenotypic requirement is less clear, with conflicting reports ranging from no detectable phenotype to reduced TRAP levels and impaired hepatocyte infectivity."},"narrative":{"mechanistic_narrative":"POFUT2 (PF3D7_0909200) is a GDP-fucose protein O-fucosyltransferase that O-glycosylates thrombospondin type I repeat (TSR)-containing sporozoite surface proteins, including CSP and TRAP, and its activity governs the folding, stability, and trafficking of these adhesins required for the mosquito and liver stages of the malaria life cycle [PMID:28916755]. In P. falciparum, genetic disruption of POFUT2 destabilizes and mistraffics TSR-bearing proteins, placing the enzyme within a non-canonical glycosylation-dependent ER protein quality control mechanism, and attenuates ookinete midgut colonization, sporozoite gliding motility, cell traversal, hepatocyte invasion, and exoerythrocytic development [PMID:28916755]. The phenotypic requirement diverges across species: in P. berghei, one study found null mutants with no motility defect and normal blood-stage infection [PMID:31334132], whereas another reported reduced TRAP levels, impaired gliding, and diminished hepatocyte infectivity with normal blood and mosquito stages, and molecular dynamics indicated O-fucosylation stabilizes the TSR domain structure without altering heparin binding [PMID:38421807]. Beyond these genetic and structural analyses, the enzymatic details of POFUT2 catalysis have not been characterized in the available corpus.","teleology":[{"year":2003,"claim":"Before any Plasmodium-specific function was known, the question was how POFUT2 relates to other fucosyltransferases; sequence analysis placed it in a fucosyltransferase superfamily sharing conserved motifs, framing it as a candidate O-fucosyltransferase.","evidence":"Phylogenetic analysis and conserved peptide motif identification across fucosyltransferase families","pmids":["12966037"],"confidence":"Low","gaps":["Computational/comparative only — no in vitro or in vivo functional experiment on the Plasmodium protein","Enzymatic activity and substrate specificity not tested","No cellular localization or life-cycle role established"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"claim":"The central question of what POFUT2 does in the parasite was answered by showing it O-fucosylates the TSR proteins CSP and TRAP, and that this modification is required for their stability, trafficking, and for transmission-relevant stages of the life cycle.","evidence":"Genetic knockout in P. falciparum with life-cycle-wide phenotyping (motility, traversal, hepatocyte invasion, humanized-mouse infection) plus assessment of CSP/TRAP stability and trafficking","pmids":["28916755"],"confidence":"High","gaps":["In vitro enzymatic characterization (kinetics, GDP-fucose donor use) not reported","Full repertoire of TSR-protein substrates beyond CSP and TRAP not defined","Molecular details of the ER quality-control link not resolved"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2019,"claim":"To test whether the P. falciparum requirement generalizes, POFUT2 was disrupted in the rodent model P. berghei; the null mutant showed no motility defect and normal blood-stage infection, indicating O-fucosylation is not essential in this species.","evidence":"Null-mutant generation in P. berghei with sporozoite motility assays and mouse infection","pmids":["31334132"],"confidence":"Medium","gaps":["Single-lab result that contradicts P. falciparum findings and a later P. berghei study","TRAP/CSP protein levels not quantified in this study","Reason for species divergence not explained"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2024,"claim":"A second P. berghei study revisited the requirement and found that POFUT2 disruption reduces TRAP levels and impairs gliding and hepatocyte infectivity, with MD simulation indicating O-fucosylation stabilizes the TSR fold rather than affecting heparin binding.","evidence":"POFUT2 knockout in P. berghei with TRAP quantification, gliding and invasion assays, and all-atom MD simulation of the TSR domain","pmids":["38421807"],"confidence":"Medium","gaps":["Partially contradicts the earlier P. berghei report; source of discrepancy unresolved","MD simulation is computational and hypothesis-generating, not experimental structure","Direct enzymatic modification of TRAP not biochemically demonstrated here"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":null,"claim":"The biochemical basis of POFUT2 catalysis and the source of the P. berghei phenotypic discrepancy remain unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No in vitro reconstitution of POFUT2 enzymatic activity or donor/acceptor kinetics","No experimental structure of POFUT2 or the enzyme-substrate complex","Species divergence between P. falciparum requirement and conflicting P. berghei reports not mechanistically explained"],"attribution":[]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":["CSP (CIRCUMSPOROZOITE PROTEIN) — TSR-CONTAINING SUBSTRATE O-FUCOSYLATED BY POFUT2 [#1]","TRAP (THROMBOSPONDIN-RELATED ANONYMOUS PROTEIN) — TSR-CONTAINING SUBSTRATE O-FUCOSYLATED BY POFUT2 [#1, #3]"],"other_free_text":["O-fucosylation of TSR domains supports folding, stability, and ER-dependent trafficking of TSR-bearing sporozoite surface adhesins in P. falciparum [#1].","Loss of POFUT2 attenuates ookinete midgut colonization and impairs sporozoite gliding motility, cell traversal, and hepatocyte invasion in P. falciparum [#1].","Phenotypic requirement diverges across species: no essential role reported in one P. berghei study [#2] versus reduced TRAP and impaired hepatocyte infectivity in another [#3].","MD simulation indicates O-fucosylation stabilizes the TSR domain fold rather than affecting heparin binding [#3]."]}},"prefetch_data":{},"corpus_meta":[{"pmid":"12966037","id":"PMC_12966037","title":"A new superfamily of protein-O-fucosyltransferases, alpha2-fucosyltransferases, and alpha6-fucosyltransferases: phylogeny and identification of conserved peptide motifs.","date":"2003","source":"Glycobiology","url":"https://pubmed.ncbi.nlm.nih.gov/12966037","citation_count":56,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"28916755","id":"PMC_28916755","title":"Protein O-fucosylation in Plasmodium falciparum ensures efficient infection of mosquito and vertebrate hosts.","date":"2017","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/28916755","citation_count":52,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["POFUT2"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"23615908","id":"PMC_23615908","title":"Biosynthesis of GDP-fucose and other sugar nucleotides in the blood stages of Plasmodium falciparum.","date":"2013","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/23615908","citation_count":36,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["GDP"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"31334132","id":"PMC_31334132","title":"Protein O-Fucosyltransferase 2 Is Not Essential for Plasmodium berghei Development.","date":"2019","source":"Frontiers in cellular and infection microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/31334132","citation_count":12,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["POFUT2"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"38421807","id":"PMC_38421807","title":"Protein O-Fucosyltransferase Is Required for the Efficient Invasion of Hepatocytes by Plasmodium berghei Sporozoites.","date":"2024","source":"ACS infectious diseases","url":"https://pubmed.ncbi.nlm.nih.gov/38421807","citation_count":5,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["POFUT2"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":4995,"output_tokens":1438,"usd":0.018277,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6408,"output_tokens":2610,"usd":0.048645,"stage2_stop_reason":"end_turn"},"total_usd":0.066922,"stage1_batch_id":"msgbatch_01DisAaTypwmC8QwdMBuePHo","stage2_batch_id":"msgbatch_0184zxZTqxiEfdYYfPMfkqjb","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2003,\n      \"finding\": \"POFUT2 (protein O-fucosyltransferase family 2) was identified as a member of a new superfamily of fucosyltransferases sharing three conserved peptide motifs with alpha2-fucosyltransferases, alpha6-fucosyltransferases, and POFUT1, suggesting origin from a common ancestor by gene duplication and divergent evolution.\",\n      \"method\": \"Phylogenetic analysis and identification of conserved peptide motifs across fucosyltransferase families\",\n      \"journal\": \"Glycobiology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 4 / Weak — computational/comparative sequence analysis only, no in vitro or in vivo functional experiment performed on the Plasmodium POFUT2 protein itself\",\n      \"pmids\": [\"12966037\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"POFUT2 (PF3D7_0909200) is the Plasmodium O-fucosyltransferase responsible for O-glycosylating the thrombospondin repeat (TSR)-containing sporozoite surface proteins CSP and TRAP. Genetic disruption of POFUT2 in P. falciparum produced ookinetes attenuated for mosquito midgut colonization, and POFUT2-deficient sporozoites were impaired for gliding motility, cell traversal, hepatocyte invasion, and production of exoerythrocytic forms in humanized chimeric liver mice. These defects were attributed to destabilization and incorrect trafficking of TSR-bearing proteins, placing POFUT2 in a non-canonical glycosylation-dependent ER protein quality control mechanism.\",\n      \"method\": \"Genetic disruption (knockout) of POFUT2 in P. falciparum; phenotyping across the full parasite life cycle; assessment of CSP/TRAP stability and trafficking\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — clean genetic knockout with multiple orthogonal phenotypic readouts (motility, invasion, trafficking, in vivo infection) across distinct life-cycle stages; mechanistic link to TSR protein quality control established\",\n      \"pmids\": [\"28916755\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"POFUT2 null-mutant P. berghei parasites showed no deleterious motility phenotypes and successfully established blood-stage infection in mice, indicating that POFUT2-mediated O-fucosylation of TSR domains is not essential for P. berghei development in contrast to findings in P. falciparum.\",\n      \"method\": \"Genetic disruption (null mutant generation) of POFUT2 in P. berghei; full life-cycle phenotyping including sporozoite motility assays and mouse infection\",\n      \"journal\": \"Frontiers in cellular and infection microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — clean genetic knockout with multiple phenotypic assays in a rodent malaria model, but contradicts P. falciparum findings and one subsequent P. berghei study; single-lab result\",\n      \"pmids\": [\"31334132\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium berghei\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"Disruption of POFUT2 in P. berghei resulted in sporozoites with reduced TRAP protein levels, impaired gliding motility, and diminished hepatocyte infectivity in mice, while blood and mosquito stages developed normally. All-atom molecular dynamics simulation suggested O-fucosylation stabilizes the TSR domain structure rather than affecting its heparin-binding capacity.\",\n      \"method\": \"POFUT2 gene disruption (KO) in P. berghei; quantification of TRAP protein levels; gliding motility and hepatocyte invasion assays; all-atom MD simulation of TSR domain\",\n      \"journal\": \"ACS infectious diseases\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genetic knockout with mechanistic follow-up (TRAP quantification, motility assay, invasion assay) in a rodent malaria model; MD simulation is computational and hypothesis-generating; single lab, partially contradicts PMID:31334132\",\n      \"pmids\": [\"38421807\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium berghei\", \"strain\": \"\"}\n      ]\n    }\n  ],\n  \"current_model\": \"POFUT2 (PF3D7_0909200) is a GDP-fucose protein O-fucosyltransferase that O-glycosylates thrombospondin type I repeat (TSR)-containing proteins, including the sporozoite surface proteins CSP and TRAP; in P. falciparum, this modification is required for proper TSR protein folding, stability, and ER-dependent trafficking, and its loss severely attenuates mosquito midgut colonization, sporozoite gliding motility, hepatocyte invasion, and liver-stage development, whereas in P. berghei the phenotypic requirement is less clear, with conflicting reports ranging from no detectable phenotype to reduced TRAP levels and impaired hepatocyte infectivity.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"POFUT2 (PF3D7_0909200) is a GDP-fucose protein O-fucosyltransferase that O-glycosylates thrombospondin type I repeat (TSR)-containing sporozoite surface proteins, including CSP and TRAP, and its activity governs the folding, stability, and trafficking of these adhesins required for the mosquito and liver stages of the malaria life cycle [#1]. In P. falciparum, genetic disruption of POFUT2 destabilizes and mistraffics TSR-bearing proteins, placing the enzyme within a non-canonical glycosylation-dependent ER protein quality control mechanism, and attenuates ookinete midgut colonization, sporozoite gliding motility, cell traversal, hepatocyte invasion, and exoerythrocytic development [#1]. The phenotypic requirement diverges across species: in P. berghei, one study found null mutants with no motility defect and normal blood-stage infection [#2], whereas another reported reduced TRAP levels, impaired gliding, and diminished hepatocyte infectivity with normal blood and mosquito stages, and molecular dynamics indicated O-fucosylation stabilizes the TSR domain structure without altering heparin binding [#3]. Beyond these genetic and structural analyses, the enzymatic details of POFUT2 catalysis have not been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2003,\n      \"claim\": \"Before any Plasmodium-specific function was known, the question was how POFUT2 relates to other fucosyltransferases; sequence analysis placed it in a fucosyltransferase superfamily sharing conserved motifs, framing it as a candidate O-fucosyltransferase.\",\n      \"evidence\": \"Phylogenetic analysis and conserved peptide motif identification across fucosyltransferase families\",\n      \"pmids\": [\"12966037\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Computational/comparative only \\u2014 no in vitro or in vivo functional experiment on the Plasmodium protein\",\n        \"Enzymatic activity and substrate specificity not tested\",\n        \"No cellular localization or life-cycle role established\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"The central question of what POFUT2 does in the parasite was answered by showing it O-fucosylates the TSR proteins CSP and TRAP, and that this modification is required for their stability, trafficking, and for transmission-relevant stages of the life cycle.\",\n      \"evidence\": \"Genetic knockout in P. falciparum with life-cycle-wide phenotyping (motility, traversal, hepatocyte invasion, humanized-mouse infection) plus assessment of CSP/TRAP stability and trafficking\",\n      \"pmids\": [\"28916755\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"In vitro enzymatic characterization (kinetics, GDP-fucose donor use) not reported\",\n        \"Full repertoire of TSR-protein substrates beyond CSP and TRAP not defined\",\n        \"Molecular details of the ER quality-control link not resolved\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"To test whether the P. falciparum requirement generalizes, POFUT2 was disrupted in the rodent model P. berghei; the null mutant showed no motility defect and normal blood-stage infection, indicating O-fucosylation is not essential in this species.\",\n      \"evidence\": \"Null-mutant generation in P. berghei with sporozoite motility assays and mouse infection\",\n      \"pmids\": [\"31334132\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Single-lab result that contradicts P. falciparum findings and a later P. berghei study\",\n        \"TRAP/CSP protein levels not quantified in this study\",\n        \"Reason for species divergence not explained\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"A second P. berghei study revisited the requirement and found that POFUT2 disruption reduces TRAP levels and impairs gliding and hepatocyte infectivity, with MD simulation indicating O-fucosylation stabilizes the TSR fold rather than affecting heparin binding.\",\n      \"evidence\": \"POFUT2 knockout in P. berghei with TRAP quantification, gliding and invasion assays, and all-atom MD simulation of the TSR domain\",\n      \"pmids\": [\"38421807\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Partially contradicts the earlier P. berghei report; source of discrepancy unresolved\",\n        \"MD simulation is computational and hypothesis-generating, not experimental structure\",\n        \"Direct enzymatic modification of TRAP not biochemically demonstrated here\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The biochemical basis of POFUT2 catalysis and the source of the P. berghei phenotypic discrepancy remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No in vitro reconstitution of POFUT2 enzymatic activity or donor/acceptor kinetics\",\n        \"No experimental structure of POFUT2 or the enzyme-substrate complex\",\n        \"Species divergence between P. falciparum requirement and conflicting P. berghei reports not mechanistically explained\"\n      ],\n      \"attribution\": []\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0046922\", \"supporting_discovery_ids\": [1, 3]},\n      {\"term_id\": \"GO:0008417\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005783\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0036065\", \"supporting_discovery_ids\": [1, 3]},\n      {\"term_id\": \"GO:0034976\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\n      \"CSP (circumsporozoite protein) \\u2014 TSR-containing substrate O-fucosylated by POFUT2 [#1]\",\n      \"TRAP (thrombospondin-related anonymous protein) \\u2014 TSR-containing substrate O-fucosylated by POFUT2 [#1, #3]\"\n    ],\n    \"other_free_text\": [\n      \"O-fucosylation of TSR domains supports folding, stability, and ER-dependent trafficking of TSR-bearing sporozoite surface adhesins in P. falciparum [#1].\",\n      \"Loss of POFUT2 attenuates ookinete midgut colonization and impairs sporozoite gliding motility, cell traversal, and hepatocyte invasion in P. falciparum [#1].\",\n      \"Phenotypic requirement diverges across species: no essential role reported in one P. berghei study [#2] versus reduced TRAP and impaired hepatocyte infectivity in another [#3].\",\n      \"MD simulation indicates O-fucosylation stabilizes the TSR domain fold rather than affecting heparin binding [#3].\"\n    ]\n  }\n}\n```","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0909200","name":null,"product":"GDP-fucose protein O-fucosyltransferase 2","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0810400","name":null,"product":"GDP-fucose protein O-fucosyltransferase 2","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0707200","name":null,"product":"GDP-fucose protein O-fucosyltransferase 2, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"POFUT2","evaluation":null}